This is a default text for your page Tetrahydroprotoberbine N-methyltransferase Protein. Click above on edit this page to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

Function

The protein being studied, Tetrahydroprotoberbine N-methyltransferase, is found in yellow horned poppy (Glaucium Flavum). The function of the protein is substate recognition as well as catalysis for the ration engineering of enyzmes for chemoenzymatic synthesis and metabolic engineering. The relative activity of 8 and more substrates were tested. Protoberberine had the highest percentage.

Disease

Relevance

Studying Tetrahydroprotoberbine will provide commercial application where one will gain a lot of knowledge from both the research paper and online sources. Studying this protein will allow readers to engage in the material and apply their own knowledge to better understand the study. This research will provide descriptive roles that TNMT plays such as pathway leading to the formation of different substrates including Protoberberine. ^[3]

Structural highlights

This scene displays the catalytic triad which are the amino acids His-208, Glu-204, and Glu-207. The authors explained within the paper that other amino acids may play a role in the triad as well. They were unsure but those three were the most accurate. These amino acids play an important role in catalysis for the protein.

This scene displays the spacefill view of Tetrahydroprotoberbine. This view allows viewers to see the different colored elements such as carbon(grey), nitrogen(blue), and oxygen(red).

This scene displays the ligand of the protein. The ligand of the protein is named SAM.

This scene displays the active site of my the protein. In green, there is Alanine, in yellow Asparatic Acid, and in blue Valine.